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Naji, M. |
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Motta, Antonella |
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Aletan, Dirar |
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Mohamed, Tarek |
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Ertürk, Emre |
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Taccardi, Nicola |
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Kononenko, Denys |
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Petrov, R. H. | Madrid |
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Alshaaer, Mazen | Brussels |
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Bih, L. |
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Casati, R. |
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Muller, Hermance |
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Kočí, Jan | Prague |
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Šuljagić, Marija |
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Kalteremidou, Kalliopi-Artemi | Brussels |
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Azam, Siraj |
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Ospanova, Alyiya |
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Blanpain, Bart |
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Ali, M. A. |
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Popa, V. |
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Rančić, M. |
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Ollier, Nadège |
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Azevedo, Nuno Monteiro |
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Landes, Michael |
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Rignanese, Gian-Marco |
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Matias, Pedro M.
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Topics
Publications (8/8 displayed)
- 2020Redox-Polymer-Wired [NiFeSe] Hydrogenase Variants with Enhanced O Stability for Triple-Protected High-Current-Density H-Oxidation Bioanodescitations
- 2020Redox-Polymer-Wired [NiFeSe] Hydrogenase Variants with Enhanced O2 Stability for Triple-Protected High-Current-Density H2-Oxidation Bioanodescitations
- 2020Redox-polymer-wired [NiFeSe] hydrogenase variants with enhanced O(_2) stability for triple-protected high-current-density H(_2)-oxidation bioanodes
- 2016A putative siderophore-interacting protein from the marine bacterium Shewanella frigidimarina NCIMB 400citations
- 2015Superoxide reductase from Giardia intestinaliscitations
- 2011Superoxide reductase from Nanoarchaeum equitans: expression, purification, crystallization and preliminary X-ray crystallographic analysiscitations
- 2010Purification, crystallization and X-ray crystallographic analysis of Archaeoglobus fulgidus neelaredoxincitations
- 2010Cloning, purification, crystallization and X-ray crystallographic analysis of Ignicoccus hospitalis neelaredoxincitations
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article
A putative siderophore-interacting protein from the marine bacterium Shewanella frigidimarina NCIMB 400
Abstract
<p>Siderophore-binding proteins (SIPs) perform a key role in iron acquisition in multiple organisms. In the genome of the marine bacterium Shewanella frigidimarina NCIMB 400, the gene tagged as SFRI-RS12295 encodes a protein from this family. Here, the cloning, expression, purification and crystallization of this protein are reported, together with its preliminary X-ray crystallographic analysis to 1.35 Å resolution. The SIP crystals belonged to the monoclinic space group P21, with unit-cell parameters a = 48.04, b = 78.31, c = 67.71 Å, α = 90, β = 99.94, γ = 90°, and are predicted to contain two molecules per asymmetric unit. Structure determination by molecular replacement and the use of previously determined ∼2 Å resolution SIP structures with ∼30% sequence identity as templates are ongoing.</p>